Electrophoresis R . D. Strickland, Research Service, Veterans Administration Hospital, Albuquerque, New Mexico
T
title of this review has been changed from “Electrochromatography” to “Electrophoresis” because a survey of the literature shows a n overwhelming preference for the latter term. This preference seems logical because the resemblance b e h e e n electrophoresis and chromatography is mainly superficial, being related t’o the accident’al similarity of the patterns formed by the separated materials rather than to the fundamental principles underlying the separations. The term electrochromatography is also undesirable because it tends to esclude from consideration by a reviewer the important’ subject of free solution electrophoresis, a method that’ does not resemble chromatography a t all. There has been a marked diminution in the practice of coining new terms to ident’ify the method of electrophoresis; the neologisms listed in the previous review appear to be falling into disuse. It has become customary to identify the kind of electrophoresis by adding some charact’erizing word or prefis to the generic term-eg., paper electrophoresis. The identifying term may refer to the apparatus (column elect’rophoresis) t’o the medium (agar electrophoresis), to the mode of sample detection (radioelectrophoresis), ‘to the mode of applying electrical power (“crossed-current” electrophoresis) , or to t’he direct.ion of sample migration (vertical electrophoresis, t,wo-dimensional electrophoresis) ; a number of other such categorizations could be cited. Ai less haphazard system of nomenclature would clearly be desirable, but the current practice causes little difficulty escept when the identifying term is made into a prefix such as radio- or iono-; in these instances the keyword is in danger of becoming lost in the abst’ract lit’erature. The coinage “immunoelectrophoresis” is now so widely used that, it’ has become a useful keyword in it,sown right. This review contains many more references than does t>he previous one. In some degree this reflects an increased use of electrophoret’ic methods, but i t is also owing to the inclusion of many citations to literature in journals or languages that are not ordinarily read 11y English-speaking rhemists. Such references have been incorporated whenever less esotic esamples of valuable trchniques, applic.ations, or ideas have heen lacking. Whenever obscure citations have been used, the Chemical HE
~
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Abstracts reference has been appended to the journal reference. The large majority of electrophoretic applications remain in the general realm of biochemistry. There has been a noticeable increase in application of the method to biological substances other than blood serum. This review contains a few supplementary citations from the years 195760, but its principal scope estends from the latter part of 1961 through the first half of 1963. BOOKS AND REVIEWS
I n addition to books describing paper electrophoresis (2.21, 257, 756), there have appeared books concerned with the techniques of high voltage electrophoresis (170) and the subject of separations of inorganic substances
(474)’ The range of electrophoretic literature has grown so large that the topics for reviews have tended toward extreme specialization: There are two brief reviews devoted to zone electrophoresis (105, 176) and one devoted to the problems in the electrophoretic separation of proteins (769); by contrast the special subject of immunoelectrophoresis has been reviewed extensively (59, 65, 505, 605, 659, 999). There are literature surveys relating to varieties of media, including paper (339, 349), starch blocks for preparative work (163), starch gel, ( 2 3 ) , synthetic gels ( l o r ) , and free solutions (151). Two reviews are devoted to radiochemical applications (55, 872), one to forensic uses (865), one to the analysis of tissue proteins ( 6 0 ) , and one to the electrophoretic and immunological properties of milk (72). Reviews that have specifically clinical interest include such topics as cancer diagnosis by polarography (748),blood plasma in bacterial infections (643), serum proteins in helminthic diseases (480), proteins in cerebrospinal fluid (818), body fluids in the Kimmelstiel-Wilson syndrome (302), the measurement of thyrosine-binding proteins in serum (717), and investigations of the mechanisms of fibrinolysis (354). FUNDAMENTAL DEVELOPMENTS
Many papers not cited in this section contain contributions to the theory of electrophoreqis or include systematic studies basic to the operation of electro-
phoretic systems. The variety of such contributions is so great that it seems preferable in the interests of coherence to mention them within appropriate categories in the main body of this review. There has been a theoretical analysis of the effects of rtabilizing media upon zone mobility and spreading (311) and moving boundary electrophoresis has been described in termh of mathematically induced analogs ( 8 7 ) . A treatment has been devised that allows the study of chemical interactions through the evaluation of the effects upon boundary patterns of alternating electrical fields (129); a n analysis of the effects of intermittent current upon electrophoretic mobility in free solution is available (601). One paper discusses electrophoresis in relation to surface conductance (SIO), while another is concerned with surface charge effects (352). There have been systematic studies of the effects of chemical (614) and physical (615) variables upon the patterns obtained by fractionating the proteins of serum and a n investigation relating such variables to electrophoretic mobility (409). There has been a discussion of the function of low molecular weight ampholytes in the electrophoretic separation of proteins (839). Immunoelectrophoresis has been analyzed theoretically (16). APPARATUS
The number of new apparatus for analytical electrophoresis in gels (79, 579, 619, 6.96, 880, 881) indicates the growing interest in this kind of medium; in several instances the apparatus for gels is designed to be used on the microscale (190, 669, 690, 882) and there is one for electrophoresis in two dimensions (697). Two-dimensional migration is also accomplished on paper (709, 727). Several improved high voltage systems have been described (79, 228, 579, 584, 619, 632, 706, 881). ;2mong new apparatus for use with filter paper are one for vertical migration ( 8 6 ) ,one that augments electromigration with centrifugal force (536), and one that has been partially automated (380). A new compact free solution apparatus has been described (916 ) . Improvements in conventional apparatus include a means of regulating the moisture content of paper strips by uniform pressure supplied by a rubber bladder inflated with coolant ( 5 6 ) , a
means of temperature control (240), series connected potentiometers for current regulation (594),and the use of a super-imposed alternating current which is said to improve resolution
(814). h number of densitometers for scanning electrophorograx s have been described (82, 720, 825, 943)) including ones t h a t record, irit'egrate, or are otherwise automated (78, 237, 428, 957). The use of interference filters in densitometry has been discussed (669). Other measuring deiices include a n automatic recording refract'ometer (517 ) a schlieren scanr!er for agar ( 6 @ ) , a polarographic attachment (138), and a semiautomatic device for locating and counting radioactive .,pots on a twodimensional pattern 11566).,i device for generating complex density gradients is described (421). Preparative apparatus for batches of material has undergone a number of interesting improvements, including the use of semipermeable barriers (70, 422, 627, 751, 888) and the use of gels (229, 705) with arrangements for the elution of samples (246 578). Countercurrent electrophoresis on paper is used for preparative purposes (243, 244, 245, 267). Most apparatus for preparative electrophoi-esis make use of the continuous principle (32) 68, 90, 341, 374, 462, 477, 679, 750) that depends upon allowing buffer and sample to flow a t right angle:, to a n electrical field; usually the supporting medium is paper, but such separations can be made in free solution ( 9 l 7 ) . ~
powder (359), polyvinyl (573), poly(methyl met'hacrylate) (324),and powdered glass (372). St,arch gel is difficult to prepare, but there is little doubt t h a t the best resolutions of biological mistures are obtained in this substance (85). Some of its resolving power is owing to gel filtration effects (810). A number of valuable contributions to techniques for using starch gel have been made (37, 164, 186, 271, 348, 447, 611). Pevikon C-870 can be combined with starch gel ~:108,109). Aigar contains acidic groups which cause adsorption of samples and coniiribute to electroendosmo 1,o overcome this objectionable property include the use of agaroee, a nonacidic derivative of agar (309, 370, 371), and the use of a barium-treated agar (379). .i number of improved techniques for using agar gel have been published (119, 127, 149, 157,628). Polyacrylamide gels are being used increasingly in spite of the technical difficulties entailed in their preparation. .i number of descriptions of their use (621, 698, 699, 704, 813, 918) and studies demonstrating their usefulness (35,363,405,553,628)are available. Ion exchange paper (29, 824), ion exchange membranes (345), and ion exchange resins (136) have the property of preventing the movement of samples in response to buffer flow or turbulence but allowing electromigration to occur. It' is the opinion of this reviewer t h a t there is unusual promise for important developments involving this variety of supporting medium.
STABILIZING MEDIA
A comparison has been made between moving boundary and zone electrophoresis (793). Free solution electrophoresis and electrophoresis stabilized by density grad..ents give similar results (518) and density gradient systems can be used for measuring mobilities ( 2 ) . Paper is still by far the most commonly used supporting medium, but there is growing evidence t h a t cellulose acetat,e films give better resolution and are easier to use (9, 515, 442, 504, 546, 575, 590, 613, 648). Detailed instructions for electrophoresis on cellulose acetate have been published (285). Fiber glass paper has heen used for the separation of inorganic ions dissolved in fused salts (20). High volt'age electropharesis has been axomplished on rayon acetate fabric (91.4). T h e results of electrophoresis of serum proteins in agar, on paper, and in free solution (4.90),and the results of electrophoresis of cerebral tissue proteins on paper, cellulcse acetate, and agar gel ($10) have been compared. Among the powders or granular materials t'hat have been used as supporting media are starch (266),cellulose
BUFFERS
Electrophoretic separations are great,ly influenced by p H (92, 165, 183, 484, 761). The efficiencies of various buffers have been compared (250: 272, 454, 608); the effects of ionic strengt'h, using veronal buffer, upon electrophoretic behavior have heen studied systematically (786). Tris(hydrosymethy1)aminomethane buffer has been proposed for moving boundary electrophoresis (777), and, when modified by the addition of borate, for paper electrophoresis of proteins (9,9). Phenolacetic acid is a good buffering agent for separating nucleic acids and proteins ( 5 2 ) . Formic and acetic acids with pyridine make a useful buffer for separating amino acids (258). The effects of adding urea to buffers for protein separations (531, 672, 835), alburnin to the buffer for lipoprotein separations (476), phosphate to borate buffers (SOY),and calcium to buffers for protein separations (719) have been studied. PROCEDURES
Manipulative Techniques.
Dilute .sample solutions such as cerebrospinal
fluid (I 7 3 ) ,gastric juice (S92),and urine (357) can be concentrated and protein solutions can be w s h e d free of salt (71) as preliminaries to electrophoresis. There is a simple technique for separating the serum from microliter amounts of blood by centrifugation ( 6 9 ) . Methods for applying samples to paper (668), to starch blocks (725))and to agar gel (883) have been proposed. Background st'ain can be removed from acrylamide gels by applying a n electrical current (261, 262). Methods have been described for extracting dyed proteins from paper (780, 875), from cellulose acetate (467), from agar (581), and from starch gel (869). Detachable auxiliary sheets have been used to detect' the pathways of protein fractions during cwnt,inuous electrophoresis (629). Starch gel electrophorograms can be copied by making contact prints (403) or they can be processed into thin transparent plastic film (73, 33.5, 337). There is ti device that f a d i t a t e s the staining of paper strips (903). Detection and Measurement. T h e measurement of proteins by the amounts of dye that they are capable of binding has been studied critically with respect to the effects of denaturation ( 4 9 5 ) , the effects of p H and salts on binding capacity (lid), the varying affinities between dyes and proteins (187, 746), and the effects of albumin trailing (617). Comparative studies of the relative merits of elution and of direct densitometry have been made (134, 445,889). There is a way to calculate the amounts of two incompletely separated fractions (457), a n arithmetic way to correct for densitometric: errors ( 1 3 4 , and a mathematical treatment for locating the peaks of fractions when these are hard to detect visually (456). Stains t h a t have been used for measuring proteins inrlude Amido Black (13, 14, 41, l 2 8 ) , 151-omophenol T3lue (130, 227, goo), Ponceau S (442), Xaphthalene Black 1013 (54),I3romocresol Green (166), I3romothymol Blue (224), Light Green S. F. (905), Procion I3rilliant I3lue RS or Cooniassie T3rilliant Dlue R250 (256), and Fluoresccxin isot,hiocyanate (287). Phosphomolybdate can be used t o develop colors in protein electrophorograms (285). Macroglobulinemia can he det,erted by treating serum with penadlamine before electrophoresis (473). I3etaglobulins can be suhfractionated (.hemically by means of precii)itants (468). Radiographic methods hsve been used to detect samplcs in microelectrophoretic patterns (801), immunoelectrophoretic patterns (375),zinc-complexed serum proteins (318). and Ion. concentrations of protein (2::)). 11ethods for meawring serum lipoVOL. 36, N O 5, APRIL 1964
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proteins have been compared (626). Dyes used for staining lipoproteins include Sudan Black (110, 860, 879), Sudan Black U (712), Sudan Black HB or Ceres Black (541), Sudan Blue (535), Sudan I1 or Sudan 111 (201, 745, 852), Sudan IV (944), Rhodamine B or G (142), Cero1 Black (336),Ceres Schwarz (6181, and Orange G (41). Lipoproteins can be measured by direct spectrophotometry a t 200 and 590 mp (708), or by fluorescence (666). Phospholipides can be detected by a violet complex that they form with mercury and diphenylcarbazone (730). There have been several modifications of the periodic acid-Schiff reaction for detecting glycoproteins (233, 446, 783, 811) and a systematic study of the optimum reaction conditions ( 3 9 ) . Glycoprotein staining methods have been compared (444). Mucopolysaccharides can be stained with acriflavine (847), Alcian Blue or hzocarmine (247), and Alcian Blue or methylene blue (280); serum mucopolysaccharides can be concentrated previous to electrophoresis by precipitation with tannin and caffeine (323) and measured after electrophoresis by polarography (411 ) . Systems for separating and identifying amino acids have been proposed ( 4 5 , 4 6 , 9 8 , 258,593, 657, 760) including one for sulfur and selenium-containing amino acids (645). Trinitrobenzenesulfonic acid (792) can be used as a reagent for detecting and measuring amino acids and peptides on filter paper; phenol isothiocyanate can be used to detect peptides (803). Methods are available for separating and measuring nucleotides ( 6 1 ) , radioactive nucleotides (901), nucleic acids (235, 856), nucleoproteins (866, 876), and microsomal components (489). Many of the papers mentioned in the enzyme heading in the applications section of this review contain valuable contributions to analytical technique; the papers listed here are more or less specifically concerned with methodology. Methods have been described for detecting and measuring dehydrogenases (126, 416, 470, 492, 921), transaminases (la@, esterases (137, 637), ribonucleases (877), amylases (897), phosphatases (759, 896), fibrinolysins (365), and catalase (343). Hemoglobins can be measured spectrophotometrically in agar (931) ; Amido H a c k is a suitable stain for hemoglobin (680). Specific blood group substances can be isolated by paper electrophoresis (830). lletallic ions in starch block electrophorograms of serum can be measured by emission spectroscopy (491). Mobilities. T h e mobilities of asphaltenes in nitromethane have been measured (929). This example of a nonaqueous solvent and another involving fused salts (20) are the only ones that
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this reviewer can cite from current literature; it seems strange that such a promising area of development should be so largely neglected. h method for reporting mobilities in terms of a n internal standard has been proposed (857); there are also ways to compute corrected mobilities (458, 631, 826) and a technique for plotting mobility as a function of p H (736). The mobilities of plasma proteins at p H 7.8 (873) and the effects of varying p H upon blood protein mobilities (508) and on mercaptalbumin (167) have been reported. hlobililties have been measured by means of countercurrent electrophoresis on paper (767). The effects upon the mobility of blood proteins of bound sialic acid (768), detergents (49, 50, 230), iodinized contrast media (465), and autogenous serum factors in malignancies (728) have been studied. Methods for measuring the mobilities of particles coated with proteins (77, 153), of colloidal particles (101), and of cells (732) have been reported. Interactions. Electrophoresis is finding increasing use as a method for studying the interaction of substances. Examples of this application include the binding of thyroxine and thyroxine-like substances to proteins (33, 100, 149, 194, 254, 276, 332, 927), and the binding to serum proteins of vitamin RI2 (62, 63, 661), vitamin D, (389), antibiotics (429, 430), amines ( 8 9 ) , bilirubin (195, 848),hemoglobin (295, 440), dextran derivatives (854),dyes (277, 630, 676, 770, 820), and metal ions (242, 585, 591). The formations of an enzyme-substrate complex between pepsin and serum albumin (143) and of complexes between myosins and adenosine triphosphate (936) have been demonstrated. Antigen-antibody complexes hetween tuberculosis polysaccharides and sensitized erythrocytes (567),and a number of specific antigenantibody compleyes (255, 711) have been demonstrated. Serum proteins interact with themselves under the influence of heat (822); there is electrophoretic evidence to support the hypothesis that all serum proteins are composed of a limited number of peptides in varying arrangements (104). APPLICATIONS
Biological Fluids. Most electrophoretic investigations use human serum as the sample substance but very few body fluids have escaped consideration. Electrophoretic techniques have been used to isolate or measure proteins (160, 426, 650), paraproteins (765), glycoproteins (735), mucoproteins (615), porphyrins (260, 353, 488, 560), urobilinogen (787),qteroid conjugates (375), adrenalines (935), histamine (84), sugars (788), amino acids (259, 499), Krebs
cycle acids (269), alpha-keto acids (390), aminoisobutyric acid (@a), aminocaproic acid (802), and 5-hydroxyindolacetic acid (827) in urine. Components of saliva (232, 8 6 4 , gastric juice (289, 313, 399, 522, 641), bile (420, 819), and cattle feces (710) have been separated electrophoretically. A number of papers report separations of the proteins in cerebrospinal fluids (206, 305, 317, 415, 481). The proteins of boar semen (120) and the binding by the proteins in human semen of Zn65 ( 2 4 l ) ,also the proteins in amniotic fluid (133) and in follicular fluid (162) have been studied electrophoretically. An electrophoretic test for ovulation has been proposed (896). Rliscellaneous body fluids have been analyzed for proteins (769) including synovial fluid (653)and for proteins and protein-bound carbohydrates (753), and ascitic fluid (493), lymph (293), nasal secretions (622), and tears (58) for proteins. Milk proteins have been investigated eatensively (25-28, 211 , 461 , 524, 597,686,694, 703,890,930). Normal distributions of the proteins in human serum (166, 319, 377, 427, 626, 812, 840) and studies of the normal variations of serum proteins with respect to age (695,868)have been published. There are many reports describing variations in the distribution of serum proteins in relation to clinical conditions, including circulatory disorders (43, 159, 161, 178, 234, 391, 4@, 636, 749, 842, 874, Sob), pulmonary diseases (81, 342, 443, 453, 714,907), hepatobiliary diseases ( 1 7 , 202, 413, 509, 754, 844,885, 938, 940), diabetes ( 15 , 191 , 610, 886, 898), nephritis (675, 891), skin diseases (333, 532, 646), hypothyroidism (116, 200), cancers (172, 239,559,583, 589, 779), leukemias (263, 514, 658, 688), myelomas (40,386, 464, 911), arthritis (433, 507, 556, 644, 794, 815) , gynecological conditions (314, 381, 515, 638), surgical trauma (417), burns (731), lupus erythematosis (660), encephalomyelitis and multiple sclerosis (113), schistomatosis (689), opisthorichiasis (887), psychiatric conditions (384), syphilis (497, 715, 782), leprosy (472, 863), chronic brucellosis (4829, dysentery (486), otitis media (516) , influenza (198, 723), varicella (340), chronic diseases of childhood ( l 7 7 ) , and various diseases (394). Miscellaneous studies having clinical interest include measurements of blood albumins in various diseases (678), abnormal gamma-globulins (95, 498), abnormal alpha1-globulins (465),the effect of cortisone on dysproteinemias (620), and a comparison of the electrophoroprams from post- and antemortem serum (718). Yormal distributions of the serum proteins in cats (385), cows (721), sheep (550), swine (634, 772), monkeys ( 7 4 , hamsters ( S l ) , rodents (208),and various animals (677, 716) have been
published. Pathological or experimentally induced changes in the serum proteins of animals include those resulting from trypaniosomiasis (312), liver damage (572), and paratyphoid (845) in cows, pregnancy (291) and hyperimmunity to tetanus (655) in horses, listeriosis in sheep (34), trichinosis (438), genetically regulated protein patterns (448), and hyperimmunity to cholera (367) in swire, uremia (926), leishmaniasis (724), and hepatectomy (451) in dogs, schistosomiasis in monkeys (809), arthritis (160), diphtheria immunity (674), and tumors (126, 251,270,670) in rats, typhoid immunity (596), coccidioidomycosis (222), neurological mutation (933), and lethal x-irradiation (784) in mice, and trichinosis (778), typhoid immunity (596), and x-irradiation (695) i n rabbits. Lipoproteins in human serum (301, 483, 639, 640) have been studied in relation. to atherosclerosis (236, 418), lipidemia (545, 841), neoplasms (135, @O), mongolism (600), pneumonia (744), skin diseases (1E'9), and various diseases (11). Normal lipoprotein patterns in various laboi*atory and domestic animals (602), cows (487), dogs (862), and rats (238, ,?Os) have been reported; so have abnormalities caused by pyridoxine deficiency (325) and hypercholesterolemia (908) in rats, leukosis (823) and brucellosis (662) in cows, and various diseases in dogs (862). Serum glycoproteins in humans have been measured in normalcy (12, 252, 506), pulmonary disease (506, 624, 828), arthritis (298, 299, 828, 859), the toxemia of pregnancy (816), atherosclerosis (766), and various disemes (356, 494). Four seromucoid subfractions have been measured in h u m m serum (316). Carbohydrate-containing proteins have been studied in sheep (196) and dogs (53,862). T h e usefulness of hemoglobin electrophoresis as a means for distinguishing the kinds of anemia has led to the publication of numerous papers on this subject (188, 264, 286, 330, 382, 401, 450, 587, 799, 834, 843); there has also been interest in hemoglobin electrophoresis as a taxonomic criterion (278, 737, 846, 853). Hemoglobins from rats (687), mice (664), ar d X-irradiated dogs (833) have been investigated. There have also been studies of the nonhemoglobin constituents of red blood cells (10, 116, 154, 179, 265, 294, 351, 523,764,807,831,861). Tissue Proteins. . I n expanding field of investigation I S the electrophoresis of proteins from tissues; examples include extracts from brains (21, 54, 85, 347, 544, 554, 582, 663, 755), muscles (24, 139, 14'7, 226, 396, 428, 447, 463, 469, 611 906), kidneys (612, 734), liver (168, 197, 334, 571, 575, 832), skin (118, 5 ' 0 ) , eyes (106,
273, 502, 773),and miscellaneous tissues (~~4,331,439,539,540,681,726).
Miscellaneous Bidogical Materials. Studies on avian subjects include serum from chick embryos (29, SO), proteinbound phosphorus (534) and proteins (511, 821) from chicken serum, myogen from chickens (598), proteins in eggs (821), and nerve tissue from birds of paradise (148). Proteins from worms (76, 366, 592, '789, 790), insects (67, 344, 915), marine arthropods (182, 513), fish (878, 412, 525, 556), and amphibians (206, 207, 209, 431) have been investigated electrophoretically. Electrophoresis has been used to separate the carbohydrates and the proteins of rye (701),and the proteins of various grains (538) including wheat and barley (326), especially wheat (117, 171, 181, 212, 213, 214, 248, 327, 328, 435, 475, 928). Other studies concerned with plant materials include extracts from leaves (308, 519, 520, 603), beans (388, '741, 752), grapes (217, 276, 4 3 4 , miscellaneous plants (300, 501, 547, 616, 743), feeds (223), and organic matter from soil (322, 562, 563). Viruses ( 1 , 661) and bacteria (406) including E . coli (419, 739, 904), Salmonella paratyphi (296), B. cereus (637), diphtheria bacilli (685), mycobacteria (132), Candida albicans (93), Pseudomonas (193), and staphylococci (452) have been investigated. There has been a separation, in acrylamide gel, of the proteins of a slime mold (941). Special Biological Substances. E n zymes of animal origin including dehydrogenases (22, 47, 102, 124, 131, 358, 398, 425, 496, 858, 892, 919, 920), esterases (6,249,304, 346), phosphatases (75, tr67, 568, 635, 692, 746), transaminases (48, 80, 121, 123, 884), saccharases (103, 231, 642, 785), proteolytic enzymes (503, 548, 733, 808, 878), and carbonic anhydrase (609), as well as plant enzymes including enzymes from fungi (552, 553, 558, 565, 700, 867), from bacteria (376, 414, 887),from yeast (570, 909, 910), and from beets (408) have been popular subjects for electrophoretic investigations. Pituitary hormones (486, 580, 763, 871 , 934), insulin (3, 383), thyroid hormone (404, 798), steroid hormones (393), and entero- and urogastrone (682) also have been studied. Miscellaneous specific biological substances t h a t have been investigated include nucleic acids and nucleotides (432, 529, 722), venoms (526, 527, 588, 599, 924), clam poison (64), heparin (66), transferrin (216 , 282), fibrinogen (738), ceruloplasmin (6'71), haptoglobin ('740), sugar phosphates (654), ketoacids (586), dicarboxylic acids (43'7, 518, 942), tetronic acids (817),and complex of cytochrome C with phospholipides (702).
General
Chemical
Applications.
Electrophoresis is useful for determining completeness of reaction and degree of purification in t h e synthesis of radioactive compounds (542). Phenols and phenol carboxylic acids can be separated (6%). Applications of inorganic interest include systems for separating cations (19, 20, 152, 64'7, 870, 912), cation pairs (90, 218, 651), anions (329), and rare earth mixtures (155, 283, 679, 781), radioactive materials (8, 218, 664, 665, 796), including fission products (797). Radium isotopes ('796) can be separated; so can Te1Z7and TeIz9 ( 7 ) ; ions of the same elements in different valence states can be separated (91). The electrophoretic properties of ionic aluminum (791), nickel (574), chromium complexes (530), ruthenium complexes (795), carbonate suspensions (47l),silver bromide (837),and barium titanate (459) have been studied. Electrophoresis is beginning t o be exploited for separating and identifying drugs for pharmaceutical and forensic purposes; examples include isomers of tropanol (7'76), alkaloids (747, 894), narcotics (925),pachycarpine (893), and other substances (36,350). IMMUNOELECTROPHORESIS
Both the range of applications and the variety of techniques for immunoelectrophoresis have increased greatly during the past two years. This is not surprising, since the method combines the potential for positive identification of antigeriic substances with the capability for demonstrating many fractions that do not appear with electrophoresis alone. A number of apparatus have been constructed especially for immunoelectrophoresis; these include a patented cell (57), microapparatus (185, 804), and a n apparatus for two-dimensional separations (932). I n addition to starch and agar gels (the media usually chosen for immunoelectrophoresis), paper (268), cellulose acetate (338, 436, 468, 829), and a n acrylamide gel (35) have successfully been used. There have been discussions of methodology (606, 607) including quantitation (368, 623), staining ('75'7))measurements of lipoproteins (774, 775), and a method in which the medium is made to contain antibodies (707). The method has been found useful for studying enzymes including esterases (184, 360, 361, 849),proteolytic enzymes ( f i g s ) ,fibrinolysin (1sa),and pepsinogen (38). It has been applied t o milk (4, 269, 7 7 1 ) , to cerebrospinal fluid (205,204, 297), and to various biological fluids ( 5 , I S , 566, 460, 478, 479, 851) as well aq to tisque extracts including those from pituitary (140, 946) and adrenal (549) glands, eyes (281, 6 8 3 , VOL. 36, N O 5 , APRIL 1 9 6 4
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brain (158, 306), liver (292,229, SOS), connective tissue (284),and skin (946). It has also been used for investigating proteins that have been separated or modified by chemical reactions (141,
543,661,661, 673,713,850). The specificity of immunological reactions permits the demonstration of relationships between antigens from different sources in a way that is not possible by ordinary chemical methods; as examples it has been shown t h a t some tissue and serum proteins are identical (758, 805, 806)) that livetins in egg yolk are identical with some hen serum proteins (922), that conalbumin and transferrin differ only in the carbohydrate moiety (923), that protein distributions in serum and ascitic fluid from mice differ only with respect to the absence of a prealbumin in the latter fluid (407),that most mammal? have related alpha- and beta-protein fractions (762), that apes and men have many serum proteins in common (899), that there are inherited variations in human serum proteins (169),and that tissue transplant rejection causes variations in serum proteins (913). I t is possible to ascertain, by means of immunoelectrophoresis of their gastric contents, whether mosquitoes have fed upon humans or animals (651). Immunoelectrophoretic investigations of clinical interest include studies of proteins in relation to neoplasms (96, 320, 684, 855), abnormal proteins (51, 57, 111, 263, 521, 362, 369, 387), arthritis (144,145, 146, 174, 175, 120, 500), atherosclerosis (42), hereditary hemolytic disorders (576), nephrosis (656),diabetes (800),lupus (44),leprosy (83), skin diseases (364),tuberculosis (511), hepatitis (88, ll4] 125), and rickettsia antigens (288). Miscellaneous applications include studies of fetal proteins in rats (424)and humans (577), studies df specific proteins in a n electrophoretically homogeneous group (441, 604,666, 667), of complement (252), of proteins following the incorporation of C14-labeled amino acids (199),and of specific immune substances including antiglobulins (4OO), isohemagglutinins (397),and antibodies against pertussus (836), brucellosis (395),and Candida
albicans (94). LITERATURE CITED
(1) Aach, H. G., Arch. Jfikrobiol. 39, 253 (1961). (2) Aach, H. G., 2 . Naturjorsch. 18b, 337 (1963). (3) Abe, AI., Inokuma, K., Kawamura, M . , AIatsushima, Y . , T o k y o Jikeikai I k a Daigaku Zasshi 76, 863 (1961); CA 58, 366%. (4) Abelli, G., Minerca Ginecol. 13, 1094 (1961). (5) Abelli, G.. Jfonzt. Ostet Ginecol. 33, 212 (1962). (6) 7Achimastos, A. S., Granitsas, A. S . , l a t u r e 196, 69 (1962). 84 R
ANALYTICAL CHEMISTRY
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(831) Sueita, Y., Chanutin, A,, Proc. SOC.ECjotl. Biol. Med. 112. 72 11963). (832) Sukhomlinov, B. F., Edkina, V:’D., Yakovenko, A. N . ) Ibid., 1962, 8 ; C A 59, 7823h.
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